Biochemistry Lab Report

a. Proteins- macromolecules made of amino acids. Proteins have many functions in the body. Some sources of proteins are whole-grain cereals, dark breads,rice, beans, and meat.

Methionine and cysteine are both sulphur containing amino acids. Most proteins will contain one, or both of them at some point in the polypeptide chain. As such, many amino acids contain sulphur in some form, which is required in small amounts in the mammalian diet.

Course description: The chemistry and biological properties of amino acids, proteins, nucleic acids, lipids, carbohydrates, and vitamins. The course includes laboratory and tutorial sessions.

The diverse roles of amino acids: 1. Hormones (signaling type molecules)  Dopamine, thyroid type hormones 2. Metabolic Intermediates  Catabolic amino acids  Citrulline: key intermediate in the urea acid cycle, the pathway by which mammals excrete ammonia.  Ornithine: in urea acid cycle, precursor to arginine, disposal of nitrogen. 3. Osmotic effects (Osmolytes- organic compounds affecting osmosis, soluble in solution within a cell, play a role in maintaining cell volume and fluid balance.)  Ex: Antarctic fish utilize stores of amino acids to offset preservations of different ions. 4. Buffering Capacity  Zwitterion (means twin in German): A zwitterion is a chemical compound that is electrically neutral but carries formal positive and negative charges on different atoms. Zwitterions are polar and usually have a high solubility in water and a poor solubility in most organic solvents. o Often times the R group is charged.  Ex: Histidine (essential amino acid) the R group has a charge, pKa at pH 7.4. Modest change in pH results in change in charge; many proteins have a Histidine residue sitting in the active site. Changes ability to interact with substrate, which causes a profound change in kinetics.

Proteins are essential nutrients made up of chains of amino acids that the body uses for energy as well as to function. The two kinds of proteins are animal, and plant proteins. Animal proteins include meat, eggs, poultry, seafood, and dairy products. Most animal proteins are rich in zinc, and heme iron. One of the widely known reasons that many people feel animal proteins are important is because they contain more of a complete set of amino acids.

Biochemistry plays a vital role in the everyday life of everything natural and mechanical. Throughout the course, we gained an understanding of why having four stable covalent bonds that bond readily to elements makes carbon qualified to be the foundation of sustainable life. With this fundamental principle in mind, we continued learning by understanding the essentials of water. Water is amphipathic, so when participating in reactions water can either hydrolyze or condense the reaction. For example, the reaction converting ADP to ATP involves the condensation of water and vice versa resulting in the hydrolysis of water converting ATP to ADP. We then went on to learn about amino acids and their relationship to proteins. We discussed various

Nearly all the proteins are made from the BCAAs. Researchers show that the BCAA'S are mainly leucine and handle regulating protein synthesis.

Organisms cannot depend solely on spontaneous reactions for the production of materials because they occur slowly and are not responsive to the organism's needs (Martineau, Dean, et al, Laboratory Manual, 43). In order to speed up the reaction process, cells use enzymes as biological catalysts. Enzymes are able to speed up the reaction through lowering activation energy. Additionally, enzymes facilitate reactions without being consumed (manual,43). Each enzyme acts on a specific molecule or set of molecules referred to as the enzyme's substrate and the results of this reaction are called products (manual 43). As a result, enzymes promote a reaction so that substrates are converted into products on a faster pace (manual 43). Most enzymes are proteins whose structure is determined by its sequence of its amino acids. Enzymes are designed to function the best under physiological conditions of PH and temperature. Any change of these variables that change the conformation of the enzyme will destroy or enhance enzyme activity(manual, 43).

Kind of amino acid glutamine, which is found in our body | Glutamine nitrogen in every part of our body works | usually players and bodybuilders use it because it helps build muscle | It prevents muscle breakdown and helps new growth and helps wounds heal faster | Glutamine is found in all things food. Eating more protein than the amount usually is. Such as chicken, fish, eggs, milk, cheese, etc. |

INTRODUCTION Protein is a types of chemical that contain in our body. Protein is made up of many amino acids joined together by peptide bonds. Protein is important in diet. Protein is contained in many types of food. Our body need protein to build and repair tissues.

Structure and mechanism of alkaline phosphatase. Annu Rev Biophys Biomol Struct. 1992; 21:441-83. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/1525473

Throughout the world, chemical reactions are taking place to either achieve a specific purpose or prevent a specific outcome. These reactions can be as simple as boiling water to pour a coffee in the morning or as complex as industrial level biochemistry. Whether you are aware of it or not, you create numerous amounts of chemical reactions every day. According to the collision theory, a chemical reaction will occur if two or more molecules collide with the right amount of energy and the right orientation. The energy that is required from the collision depends on the molecules and can be referred to as activation energy.

These four biomolecules are metabolized by the animal body. Each biomolecule is broken down in a different process. The end result of each process is the creation of usable energy for the body. This energy is used to work and generate other chemical reactions that help the body move and think. Carbohydrates, lipids, proteins and nucleic acids each provide energy to different places within the body that, in turn, stimulate other chemical reactions to occur, creating a chain reaction of chemical reactions throughout the body. The metabolization of these major

Tryptophan is one of the scarcest amino acids found in nature and is fundamental to most proteins found throughout vertebrates. This amino acid is crucial for sufficient growth in infants and to maintain nitrogen balance in adults. The IUPAC name for tryptophan is (2S)-2-amino-3-(1H-indol-3-yl) propanoic acid and this amino acid is often abbreviated as “Trp” or “W.” Amino acids are a vital component of living organisms and act as building blocks for proteins. The basic structure of an amino acid consists of a hydrogen atom, an amino group, a carboxyl group, and an “R” group attached to a central carbon. The structure of the “R” group determines the function and interaction properties of the amino acid. There are twenty common amino acids that are found within the proteins of the human body, Tryptophan is one of them. Although amino acids are structural components of proteins, these macromolecule subunits are also catabolized into products that serve vital roles within the body. Tryptophan is catabolized into the serotonin, kynurenine, and plays a role in NAD/NADP synthesis. There are also various metabolic diseases that are associated with amino acid, caused by deficiencies and the inability to catabolize/metabolize specific amino acids. Familial hypertryptophanemia and pellagra are metabolic disorders associated with tryptophan.

The titration curve of the unknown exhibited many characteristics, such as equivalence points, pKa of ionizable groups, isoelectric point, and buffer regions, that are particularly distinct to lysine. For unclear reasons, the pH during the titration did not reach the pH for pure 0.2 M NaOH nor 0.2 M HCl and normal equivalence points expected at two extreme ends of the titration curves for all amino acids were not observed. The titration of a phosphate buffer showed that the buffer capacity is directly proportional to the molarity of the buffer. However, our results showed that although the initial pH of the phosphate buffer was less than the pKa value, the measured buffer capacity was higher towards acid than base. The accuracy of the pH meter and calibration process was questioned under assumptions that the pH of the prepared phosphate buffer was actually above pKa.